1mi7: Difference between revisions

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New page: left|200px<br /><applet load="1mi7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mi7, resolution 2.50Å" /> '''Crystal Structure of...
 
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[[Image:1mi7.gif|left|200px]]<br /><applet load="1mi7" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1mi7.gif|left|200px]]<br /><applet load="1mi7" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1mi7, resolution 2.50&Aring;" />
caption="1mi7, resolution 2.50&Aring;" />
'''Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol'''<br />
'''Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol'''<br />


==Overview==
==Overview==
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA, binding site through a pair of flexible helix-turn-helix (HTH) motifs, displayed on an intertwined helical core. Flexible N-terminal arms mediate, association between dimers bound to tandem DNA sites. The 2.5 A X-ray, structure of trpR crystallized in 30% (v/v) isopropanol reveals a, substantial conformational rearrangement of HTH motifs and N-terminal, arms, with the protein appearing in the unusual form of an ordered 3D, domain-swapped supramolecular array. Small angle X-ray scattering, measurements show that the self-association properties of trpR in solution, are fundamentally altered by isopropanol.
The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.


==About this Structure==
==About this Structure==
1MI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with IPA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1MI7 OCA].  
1MI7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=IPA:'>IPA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MI7 OCA].  


==Reference==
==Reference==
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[[Category: Benoff, B.]]
[[Category: Benoff, B.]]
[[Category: Berger, T.]]
[[Category: Berger, T.]]
[[Category: Berman, H.M.]]
[[Category: Berman, H M.]]
[[Category: Carey, J.]]
[[Category: Carey, J.]]
[[Category: Lawson, C.L.]]
[[Category: Lawson, C L.]]
[[Category: IPA]]
[[Category: IPA]]
[[Category: alcohol induced conformational rearrangement]]
[[Category: alcohol induced conformational rearrangement]]
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[[Category: domain swapping]]
[[Category: domain swapping]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:25:58 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:25 2008''

Revision as of 14:55, 21 February 2008

File:1mi7.gif


1mi7, resolution 2.50Å

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Crystal Structure of Domain Swapped trp Aporepressor in 30%(v/v) Isopropanol

OverviewOverview

The E. coli trp repressor (trpR) homodimer recognizes its palindromic DNA binding site through a pair of flexible helix-turn-helix (HTH) motifs displayed on an intertwined helical core. Flexible N-terminal arms mediate association between dimers bound to tandem DNA sites. The 2.5 A X-ray structure of trpR crystallized in 30% (v/v) isopropanol reveals a substantial conformational rearrangement of HTH motifs and N-terminal arms, with the protein appearing in the unusual form of an ordered 3D domain-swapped supramolecular array. Small angle X-ray scattering measurements show that the self-association properties of trpR in solution are fundamentally altered by isopropanol.

About this StructureAbout this Structure

1MI7 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

E. coli trp repressor forms a domain-swapped array in aqueous alcohol., Lawson CL, Benoff B, Berger T, Berman HM, Carey J, Structure. 2004 Jun;12(6):1099-108. PMID:15274929

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